ID HUM6_CAEEL Reviewed; 2098 AA.
AC P91443;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Unconventional myosin heavy chain 6;
GN Name=hum-6 {ECO:0000303|PubMed:9325109}; ORFNames=T10H10.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=9325109; DOI=10.1006/jmbi.1997.1232;
RA Baker J.P., Titus M.A.;
RT "A family of unconventional myosins from the nematode Caenorhabditis
RT elegans.";
RL J. Mol. Biol. 272:523-535(1997).
RN [3] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=10767309; DOI=10.1093/hmg/9.6.869;
RA Culetto E., Sattelle D.B.;
RT "A role for Caenorhabditis elegans in understanding the function and
RT interactions of human disease genes.";
RL Hum. Mol. Genet. 9:869-877(2000).
RN [4] {ECO:0000305}
RP INTERACTION WITH UNC-98.
RX PubMed=12808046; DOI=10.1091/mbc.e02-10-0676;
RA Mercer K.B., Flaherty D.B., Miller R.K., Qadota H., Tinley T.L.,
RA Moerman D.G., Benian G.M.;
RT "Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel
RT partner of UNC-97/PINCH in muscle adhesion complexes.";
RL Mol. Biol. Cell 14:2492-2507(2003).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250|UniProtKB:P97479}.
CC -!- SUBUNIT: Interacts with unc-98. {ECO:0000269|PubMed:12808046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13402}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; FO080098; CCD61190.1; -; Genomic_DNA.
DR PIR; T25888; T25888.
DR RefSeq; NP_508420.1; NM_076019.3.
DR AlphaFoldDB; P91443; -.
DR SMR; P91443; -.
DR BioGRID; 45484; 4.
DR IntAct; P91443; 1.
DR MINT; P91443; -.
DR STRING; 6239.T10H10.1.1; -.
DR iPTMnet; P91443; -.
DR EPD; P91443; -.
DR PaxDb; 6239-T10H10-1; -.
DR PeptideAtlas; P91443; -.
DR EnsemblMetazoa; T10H10.1.1; T10H10.1.1; WBGene00002039.
DR GeneID; 180539; -.
DR KEGG; cel:CELE_T10H10.1; -.
DR UCSC; T10H10.1; c. elegans.
DR AGR; WB:WBGene00002039; -.
DR WormBase; T10H10.1; CE13575; WBGene00002039; hum-6.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000157247; -.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; P91443; -.
DR OMA; GFQGRCR; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; P91443; -.
DR Reactome; R-CEL-2453902; The canonical retinoid cycle in rods (twilight vision).
DR PRO; PR:P91443; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002039; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0031476; C:myosin VI complex; TAS:UniProtKB.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd17092; FERM1_F1_Myosin-VII; 1.
DR CDD; cd17093; FERM2_F1_Myosin-VII; 1.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.25.40.530; MyTH4 domain; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22692:SF33; MYOSIN; 1.
DR PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR Pfam; PF00373; FERM_M; 2.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2098
FT /note="Unconventional myosin heavy chain 6"
FT /id="PRO_0000306247"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 735..757
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 758..787
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 804..833
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 929..1168
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1171..1211
FT /note="Ras-associating"
FT /evidence="ECO:0000255"
FT DOMAIN 1173..1481
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1479..1547
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1624..1772
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1778..2086
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 609..631
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 711..725
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 860..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08799"
SQ SEQUENCE 2098 AA; 239785 MW; A972E51FC54B73BB CRC64;
MVLVSKGDFI WIEPGKTEGS IPIGARVIDQ DHGRLKVIDD LGNEQWLSAD RRVRLMHPTS
VQGVEDMCQL GDFHESAILR NLFIRYREKL IYAYTGSILI AVNPYMDIAI YTADEIRMYK
RKRIGELPPH IFAIADNAYT NMRREKKNQS VIISGESGAG KTESTKLVLQ FLATISGQHS
WIEQQVLEAN PVLEAFGNAK TIRNDNSSRF GKYIDVHFNE SGSIEGAKIE QYLLEKSRIV
TQSENERNYH IFYCLLAGLS REEKSELELG TAADYYYLIQ GKTLTAEGRD DAADLAEIRS
AMRVLMINEQ EIGSIFKLLA SLLHIGNIRF RQNTNDNMES VDVADPSTLV RIAKLLQLHE
QNLLDAITTK SLVTREERVI SRLNGQQAVD ARDALAKAIY GKLFIHIVRR VNDAIYKPSQ
SRRTSIGILD IFGFENFESN SFEQLCINFA NETLQQFFVH HVFKMEQKEY DEEHINWRHI
KFVDNQATVD LIAQRPLNIL SLIDEESIFP KGTDKTMLLK LHSTHGRNEL YLQPKSELQR
AFGVTHFAGN VFYNTRGFLE KNRDSFSADL SVLISSSKMP FLARLFDDIE YDTSSRKKVT
VGNQFRRSLE QLMSQLTQTH PFFIRCIKPN EMKRALVMDR DLVLRQLRYS GMMETIKIRR
SGYPIRHDYY PFVFRYRVLV SSIQGPVNRI DLHDAAKKIC HMILGTNADY QLGKTKVFLK
DKHDLVLEQE YYRILKDKAI VIQKNVRRWL VRKDFEKQRQ AAVTIQTAWR GFDQRKRYRQ
IISGFSRLQA VLRSRQLVSH YQTLRKTIIQ FQAVCRGSLV RRQVGEKRKR GEKAPLTEVS
STASVISDSH EELVGHLFDF LPSDGKDSGN ENDSADSSRR GSYSRLHTSP VMPPANIPRV
DSYVDEDLSK YQFGKYAATF FQAQATATHV KKPLKTALLT HTEPSAQLAA LTAWTTILRF
MGDLADVKPG STNGSEVYDK TPVMIKLYAT LGKKFSAHDL EEAMLSSEYG GAKTLKKGMG
RKLISMTLKR KGKINGSDTS SISSDSVYSS FNAMLENKPM TSLDKLHYII GLGILREDLR
DEIYCQLCKQ LSNNPSKLSA ARGWILLSLC VGCFAPSERF IKYLFCFIRE RGPAGTGYSK
YIEDRLRRTQ VNGTRHQPPS YVELQANKSQ KPVVLAVTFM DGSVKTLCAD SATTAAELCK
QLAEKVGLTN SFGFSLYIAL FDKVSSLGSG TDHVMDAISQ CEQYAKEQGR QERNAPWRLF
FRKEIFSPWH DPRDDPVSTN LIYQQVIRGI KYGEYRCDKD EELAAICAQQ YYIDEGTMDV
NKLENNLPSY LPDFEMSGKE MALEKWTQTI MHQYRKKFTG RLPSQIEVKE NVVSVAKTKW
PLLFSRFYEA LKFAGPPLPK NEVIIAVNWT GVYVVDDREH VMLEFSFPEI STAYYGKGKR
STTDTCTVRT VVGDEYTFQS PNADDITNLI VMFLEGLKKR SRYLVAIKSQ KGDEKNNFLE
FEKGDLLILV NEFTGNTLLT ESVVKGENSR TCLFGLIRAE NVYVLPTLVK PSKNTLQIFP
KDMDLSLDLF NNNKQVTVVD YNAEPYTLEN FAEDNFNSQV KRVGSQISLM TLRKKESQIE
CWRFSREHID QPLLKKLNGR EDACRGAIEI FAAIMKYMGD EPSKRSRLGT HLTDHIFKLP
ISMEALRDEL YCQLVKQLTL NPSIMSEERG WELLWMATGL FAPSAALAKE ISHFLKSRPH
PIALDCQNRM QKLAKGGSRK YPPHLVEVEA IQHKTTQIFH KVFFPDNTDE AIEVDSATRA
RDFCHKIGYR LGLKSSDGFS LFVKIKDKVL AVPESEFFFD YVRSLSDWVH TNHATQKDAT
MIPINYQVYF MRKLWYNFVA GADPQADIIF HYHQESQKYL LGYHKTTKND VIELAALILR
SMTKDGKNAP LAQIPQLLDE IIPKDSLKMY SASEWRKTIS NAYARIEHLK SDQAKIEFLN
YICRWPTFGS AFFPVSQYSD LNLPDRLLLA INQTGVNIYH LDTKNLLVQY PFNVICNWTS
GNTYFNMTVG NMLKGNEGKK LLLDTTVGYK MDDLLTSYIS LLISNQNNHP SKTREVAL
//
